Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q12204

Entry ID Method Resolution Chain Position Source
AF-Q12204-F1 Predicted AlphaFoldDB

16 variants for Q12204

Variant ID(s) Position Change Description Diseaes Association Provenance
s15-375845 5 T>A No SGRP
s15-375812 16 R>G No SGRP
s15-375730 43 P>R No SGRP
s15-375713 49 H>N No SGRP
s15-375700 53 K>R No SGRP
s15-375649 70 K>R No SGRP
s15-375633 75 R>S No SGRP
s15-375517 114 S>F No SGRP
s15-375158 234 S>P No SGRP
s15-375023 279 L>F No SGRP
s15-374981 293 A>T No SGRP
s15-374882 326 I>L No SGRP
s15-374879 327 E>K No SGRP
s15-374669 397 P>S No SGRP
s15-373970 630 L>V No SGRP
s15-373886 658 T>A No SGRP

No associated diseases with Q12204

1 regional properties for Q12204

Type Name Position InterPro Accession
domain DDHD domain 519 - 700 IPR004177

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

3 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
phospholipase A1 activity Catalysis of the reaction: phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate.
phospholipase activity Catalysis of the hydrolysis of a glycerophospholipid.

4 GO annotations of biological process

Name Definition
cardiolipin metabolic process The chemical reactions and pathways involving cardiolipin, 1,3-bis(3-phosphatidyl)glycerol.
lipid catabolic process The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
phosphatidylethanolamine metabolic process The chemical reactions and pathways involving phosphatidylethanolamine, any of a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. It is a major structural phospholipid in mammalian systems. It tends to be more abundant than phosphatidylcholine in the internal membranes of the cell and is an abundant component of prokaryotic membranes.
phospholipid metabolic process The chemical reactions and pathways involving phospholipids, any lipid containing phosphoric acid as a mono- or diester.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9Y6Y8 SEC23IP SEC23-interacting protein Homo sapiens (Human) PR
Q8W5R2 SGR2 Phospholipase SGR2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MLRFTHRGLP SSTRFRNIFV RLNHIYVPWF YAIDVPNSKP YLPTYQTLHS PKKFKPFSVD
70 80 90 100 110 120
DSNRLEKASK RQERRPVLVN EDYLFKVDLS HMELSPTYWE GPTYQVRRGV WFDSSNQPLS
130 140 150 160 170 180
SDLTSEIEGL YKQLKFDDSN DDPTTTPPAE SQDIFRLKGK YPVDKENEGE QKNGSSNKDE
190 200 210 220 230 240
NESTFKFILF ANKQTAFLLS DLDGGKLQLA FLRSNLAQSL PINATMITRS YKYSSSATTK
250 260 270 280 290 300
QTSTSFKAAK TPQTEVADGS NSSKSRSIET KLEKKVSNLF NLSDFLQLFN GNASKDQDDA
310 320 330 340 350 360
QSLEKQMETD YNNADNSQGA NASSKIEDGK NSGASDRQIR SNRRDVDNLI LCVHGIGQTL
370 380 390 400 410 420
GKKYEYVNFA HTVNLLRSNM KKIYNNSEKL QSLNTAPDYK SNCNVQVLPI TWRHSISFQT
430 440 450 460 470 480
DAKEENIENP DLPTLSQVTV NGVLPLRKLL ADGLLDILLY VEPYYQDMIL QQVTSQLNKT
490 500 510 520 530 540
YRIFKEFNPE FDGKVHLVGH SLGSMILFDI LSKQKKYELE FQVDNLFFIG SPIGLLKLIQ
550 560 570 580 590 600
RTKIGDRPEF PNDLERKLTV QRPQCKDIYN VYHVCDPISY RMEPLVSKEM AHYEQTYLPH
610 620 630 640 650 660
CSEAYGLTSK VLEFGENIWK DLPGTDENNL QSKKTSPEKK EVKLSENLTR MLTGLNYTGR
670 680 690 700 710
LDYAMSPSLL EVDFISAIKS HVSYFEEPDI AAFILKEILS KHENASEIYV KRKTG